Heat and cold denaturation of β‐lactoglobulin B

FEBS Letters

Azuaga, Ana I.¹  Cortijo, M.¹  Mateo, Pedro L.¹  Galisteo, Maria L.¹  Mayorga, Obdulio L.¹ 

[1] Departamento de Quimica Fisica, Facultad de Ciencias, e Instituto de Biotecnologia, Universidad de Granada, 18071 Granada, Spain

关键词: β-Lactoglobulin B: Thermal stability;    Cold denaturation;    Guanidine hydrochloride: Scanning calorimetry;    Circular dichroism;   

DOI  :  10.1016/0014-5793(92)80784-E

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The thermal denaturation of bovine β-lactoglobulin B was investigated by high-sensitivity differential scanning microcalorimetry between pH 1.5 and 3.0 in 2OmM phosphate buffer. The process was found to be a reversible, two-state transition. Progressive addition of guanidine hydrochloride at pH 3.0 leads to the appearance of a low-temperature calorimetric endotherm, corresponding to the cold renaturation of the protein. Circular dichroism experiments have confirmed the low and high temperature denaturation processes, and have shown some structural differences between both denatured states of β-lactoglobulin B.

【 授权许可】

Unknown